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CCNH

Protein FULL name:

cyclin-H [Homo sapiens].


CCNH (Homo sapiens) is product of expression of CCNH gene.


CCNH is involved in:

DDS in Homo sapiens
     


Keywords:



FUNCTION: Regulates CDK7, the catalytic subunit of the CDK- activating kinase (CAK) enzymatic complex. CAK activates the cyclin-associated kinases CDK1, CDK2, CDK4 and CDK6 by threonine phosphorylation. CAK complexed to the core-TFIIH basal transcription factor activates RNA polymerase II by serine phosphorylation of the repetitive C-terminus domain (CTD) of its large subunit (POLR2A), allowing its escape from the promoter and elongation of the transcripts. Involved in cell cycle control and in RNA transcription by RNA polymerase II. Its expression and activity are constant throughout the cell cycle.

SUBUNIT: Associates primarily with CDK7 and MAT1 to form the CAK complex. CAK can further associate with the core-TFIIH to form the TFIIH basal transcription factor.

INTERACTION: P51948:MNAT1; NbExp=1; IntAct=EBI-741406, EBI-716139; Q96JH8:RADIL; NbExp=1; IntAct=EBI-741406, EBI-744267;

SUBCELLULAR LOCATION: Nucleus.

SIMILARITY: Belongs to the cyclin family. Cyclin C subfamily.

WEB RESOURCE: Name=NIEHS-SNPs; [LINK]


This protein can be a part of a given complexes:
NCBI GenPept GI number(s): 4502623
Species: Homo sapiens

Links to other databases:

Database ID Link
Uniprot P51946 P51946
PFAM: - P51946 (Link - using uniprot id)
InterPro: - P51946 (Link - using uniprot id)
CATH: None  
SCOP: None  
PDB: - -


Protein sequence:
MYHNSSQKRHWTFSSEEQLARLRADANRKFRCKAVANGKVLPNDPVFLEP
HEEMTLCKYYEKRLLEFCSVFKPAMPRSVVGTACMYFKRFYLNNSVMEYH
PRIIMLTCAFLACKVDEFNVSSPQFVGNLRESPLGQEKALEQILEYELLL
IQQLNFHLIVHNPYRPFEGFLIDLKTRYPILENPEILRKTADDFLNRIAL
TDAYLLYTPSQIALTAILSSASRAGITMESYLSESLMLKENRTCLSQLLD
IMKSMRNLVKKYEPPRSEEVAVLKQKLERCHSAELALNVITKKRKGYEDD
DYVSKKSKHEEEEWTDDDLVESL

CCNH (Homo sapiens) is able to recognize following damages:
CCNH (Homo sapiens) belongs to following protein families:
References:

Title Authors Journal
A novel cyclin associates with MO15/CDK7 to form the CDK-activating kinase. Fisher RP, Morgan DO Cell Aug. 26, 1994
A cyclin associated with the CDK-activating kinase MO15. Makela TP, Tassan JP, Nigg EA, Frutiger S, Hughes GJ, Weinberg RA Nature Sept. 15, 1994
Cdk-activating kinase complex is a component of human transcription factor TFIIH. Shiekhattar R, Mermelstein F, Fisher RP, Drapkin R, Dynlacht B, Wessling HC, Morgan DO, Reinberg D Nature March 16, 1995
Three-dimensional structure of human cyclin H, a positive regulator of the CDK-activating kinase. Kim KK, Chamberlin HM, Morgan DO, Kim SH Nat Struct Biol Oct. 1, 1996
The structure of cyclin H: common mode of kinase activation and specific features. Andersen G, Busso D, Poterszman A, Hwang JR, Wurtz JM, Ripp R, Thierry JC, Egly JM, Moras D EMBO J March 3, 1997
Immunoaffinity purification and functional characterization of human transcription factor IIH and RNA polymerase II from clonal cell lines that conditionally express epitope-tagged subunits of the multiprotein complexes. Kershnar E, Wu SY, Chiang CM J Biol Chem Dec. 18, 1998
Reconstitution of the transcription factor TFIIH: assignment of functions for the three enzymatic subunits, XPB, XPD, and cdk7. Tirode F, Busso D, Coin F, Egly JM Mol Cell Feb. 1, 1999
TFIIH is negatively regulated by cdk8-containing mediator complexes. Akoulitchev S, Chuikov S, Reinberg D Nature Sept. 7, 2000
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J Genome Res Oct. 1, 2004
Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M Cell Nov. 3, 2006
Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y Anal Sci Feb. 1, 2008
A quantitative atlas of mitotic phosphorylation. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP Proc Natl Acad Sci U S A Aug. 5, 2008
Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M Mol Cell Aug. 8, 2008
Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK Sci Signal Jan. 1, 2009
Large-scale proteomics analysis of the human kinome. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H Mol Cell Proteomics July 1, 2009


Last modification of this entry: Oct. 12, 2010.

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